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Forensic Chemistry

1a) Outline precautions that may be necessary to ensure accuracy and prevent
contamination of samples for analysis.
• Forensic material provides evidence in courts and so therefore needs to be
accurate as ppl’s future relies on it.
• Quality assurance ensures the correct use of scientific methods.
• They must not be contaminated during collection, storage and analysis as it leads
to incorrect conclusions.
• Clean and effective laboratory conditions are needed because if not followed, can
lead to contamination of samples.
• Suitable clothing needs o be worn.
• The area should be closed off, photograph evidence needed, measurements taken.
• Should be stored in manner to preserve conditions and when collected, the
materials should be sterilized to prevent contamination.
• Samples that could contain carbon need to be collected in a vapor-tight container.

1b) Distinguish between organic and inorganic compounds.

• Contain mostly Carbon & Hydrogen. Mainly originate from living things but can
also be manufactured.
• They combust and decompose to form CO2, CO, C.
• Include things such as hydrocarbons, alcohols and esters.

• Don’t have carbon except for metallic (ionic_ carbonates, hydrogen carbonates,
carbon oxides and carbides. Also covalent network compounds.
• Don’t decompose to form carbon and are made from natural minerals.

1c) Explain that there are different classes of carbon compounds including:
hydrocarbons, alkanols, alkanoic acids which can be identified by distinguishing

• Saturated (same homologous series)
• CnH2n+2
• Natural gas and liquid petroleum
• Functional is alkyl group
• Single bonds
• Unsaturated
• CnH2n
• Double bond
• Unsaturated.
• CnH2n-2
• Triple bond
• Formula of CnH2n+2O or CnH2n+1OH
• -OH is functional group.

• First four are water soluble
• H bonding allows for high boiling point.

Carbon Compound Functional Group Distinguishing Test
Alkane Single Add Br water in presence of
light, no reaction
Alkene Double Add Br water and colour of
Bromine changes from
brown to colourless even in
dark or light rapidly
Alkyne Triple Add Br water and colour of
Bromine changes from
brown to colourless slowly
Alkanol (can also be -OH Dry it with CaCl2 then add
oxidized) Na and Hydrogen gas is
Alkanoic Acid -COOH Add aqueous Na2CO3 and
Carbon dioxide should

1d) Explain that the inorganic chemical properties of soils and other materials may
be useful evidence.
• Soil offers important evidence for the work of forensic scientist to help solve a
crime. By testing soil samples, you can match it with the soil samples of that of
the killer. It has silt, clay, gravel etc and they vary from place to place in different
• Decaying organic matter in it is known as humus. Soil varies in colour and
chemical composition. The differences can be checked using wet and
instrumental analyses. Mass spectrometry, atomic emission spectroscopy and
• A preliminary separation takes place with a stereoscopic microscope. E.g. Insect
parts are separated (but first it is dried)
• Then mineral examination with polarized light microscopy takes place
• Particle size distribution.
• Color comparisons
• pH testing
• Groundwater tests done to find hardness or sulfate content.
• Humus content is found by heating it as it gets burnt off.
• Examination for pollen and other things.
• When soil is found on tyres or soles of feet, they are usually mixtures of other
• Glass is also useful and used in cases such as hit/run, assault. It is hard and brittle
made of metal and silicon oxides which act to modify properties of the glass. Mn
and Ni can also be used to alter the colour. It’s density and refractive media can
be used to compare glass at crime scene to glass on suspect.

1e) Discuss, suing a recent example, how progress in analytical chemistry and
changes in technology can alter the outcome of a forensic investigation.
• The technological change has altered the outcome in forensic investigation. Until
1970’s only three types of blood analyzing. 1. Identifying it is blood by ninhydrin
2. Seeing with its human or animal. 3. Identifying the blood group.
• Advances in genetic tech.
Has given genetic profiles of victim/suspect
Allows to differ people with same blood group.
• E.g. a woman was raped and murdered. Blood from the rapists hand was left on
her night gown. Both were group O but originated from different genetic
markers. The murderer was seen leaving the crime scene was a seen African-
American. This eliminated 99.7% of black male population as only 0.3% has
blood O group.
• Another woman who was convicted of killing her daughter when instead she had
been taken by a dingo. At that time there wasn’t DA testing so n samples were
kept. Etc.
• Increase in technology as allowed for AAS so now more levels of metals can be
detected and chemists can now use this to detect evidence of pollution and
prosecute the polluters.

1B) Discuss ethical issues that may need to be addressed during an analytical
• Ethics guide the conduct of person before action is taken.
• Forensic scientists have high responsibilities as their results determine the future
of a person so therefore results need to be accurate.
• They need to defend their results and conclusion well. Must also state any doubts
they have.
• Neutrality is most important. They must search for truth and not be influenced by
any other party.
• Need to commit to a code of ethics that is generally developed by their

1D) Present information summarizing a series of distinguishing tests to separate

the groups of hydrocarbons, acids bases and neutral salts in school lab and in
forensics chemists lab.

Similar as point 1b.

Class Distinguishing test Forensic chemistry example
Acid Universal indicator <7 Citric acid with gold
chloride to show
fingerprints on adhesive
Base Universal indicator >7 Cyanoacrylate (superglue)
to show fingerprints on
glass surfaces
Neutral Universal indicator 6-8 Silver nitrate to show
fingerprints on porous

• Alkane: Unreactive but go tough substitution reaction. Burns n a lot of oxygen to

make carbon dioxide and water.
• Alkenes_ addition reactions with bromine water
• Alkynes: Also addition reactions. Twice more bromine will react with one mole
of alkyne.
• Alkanols: oxidized by acid potassium dichromate to make alkanoic acid. Orange
to green.
• Alkanoic acid_ neutralized by bases to make salts and react with alkanols making
esters. Also by universal indicators.
• In labs, alkenes are distinguished with bromine water. No reaction for alkane in
room temp.
2a) Identify that carbohydrates are composed of carbon, hydrogen and oxygen
according to the formula: Cx(H20)y
• Carbohydrates = repeating sugar molecule.
• Made from C,H,O and have Cx(H20)y where x and y are different
• Classified by monomer units.
• Needed as:
-source of energy
-structure/supportive component of cell
-genetical growth/development

They come in three groups:

• Simple sugars: Such as Glucose/fructose and DNA.

Disaccharide: (dimer)
• Made when monosaccharide undergo condensation reaction (glycosidic bond)
such as sucrose or maltose. (sucrose = glucose plus a fructose and maltose = two
• Can be broken down by hydrolysis to monosaccharide.
• Water soluble and sweet tasting.
• Paper chromatography is used.
• Condensation of many monosaccharide monomers. E.g. starch, glycogen and
• Starch made from amylase (20%) and amylopectin (80%). Amylose is soluble in
water and amylopectin is branched in a coil.
• Cellulose is made of glucose and unbranched as isn’t soluble in water. It is
• Glycogen is known as animal starch and is branched.
2b) Identify glucose as a monomer and describe the condensation reactions which
-sucrose as an example of a disaccharide
-polysaccharides including glycogen, starch and cellulose.
• Glucose = monomer
• 2 monomer units by acetal linkage and condensation

C6H12O6 + C6H12O6  C12H22O11 + H2O

Glucose + fructose (isomers) = sucrose + water
• Sucrose is disaccharide formed by linking glucose and fructose together
eliminating the water.
• Polysaccharide formed by many monosaccharide and they also eliminate water
 its different arrangements form different polymers.

2c) Describe the chemical difference between reducing and non-reducing sugars.
• Reducing sugars: (monosaccharide glucose, disaccharide maltose and lactose)
act as reluctant when heated with a weak alkaline (benedicts solution) to
make orange brown precipitate of Copper (I) oxide.
• The Cu2+ ion is reduced to Cu+.
• Reaction only takes place if the carbohydrate exists in equilibrium between a
ring and open-chain form.
• Open chain = -CHO and –CO-CH2OH which are oxidize to carboxylic. R-
• Sugars in open form -CHO and –CO-CH2OH are reducing sugars as they are
easily oxidized so therefore they reduce the other reagent.
• Sucrose is non reducing because neither of the rings can convert to an open-
chain structure therefore cant form a C=O due to linkage between glucose and
fructose is carbonyl
• Sugars that have an OH attached to the same C as a ring O atom is attached to
are reducing.

2d) Distinguish between plant and animal carbohydrates composition in terms of

the presence of cellulose, starch, glycogen.
Carbohydrate Animal or Plant Fund in
Cellulose Plant Matrix structure in cell wall
Starch Plant Cytoplasm
Glycogen Animal Liver/muscle cells
• All are polymers linked by glucose units.
• Starch and glycogen (alpha glucose) are similar however glycogen is more
branched and longer.
• Cellulose (Beta glucose) is diff by its linkage of glucose units. Hydrogen bonding
make it stronger and low solubility.
• Starch made of amylose soluble (20%) and amylopectin insoluble (80%).
2A) Tests fore non reducing and reducing sugars
Compound Test
Reducing sugar Tollen’s reagent: Black precipitate or shiny
mirror when warmed
Benedict or Fehlings: Orange brown
Starch Dar blue colour when iodine added
Glycogen Add starch it goes pale pink
3a) Distinguish between proteins used for structural purposes and the uses of
proteins as enzymes.

• Proteins can be seen as primary, secondary or tertiary.

1. Primary: sequence of amino acids.
2. Secondary: tendency of polypeptides forming spirals and helical sheets depending
on the hydrogen bonds. Can be as alpha helix (wool) or beta sheets (silk).
3. Tertiary: this is its complete bonding to a specific shape and so polar, non polar
and ionic groups are stabilized.
• Proteins needed in living cells.
• There are two types – globular and fibrous
• Fibrous: tough, springy and insoluble.
• Globular: spherical and soluble in water.
• Fibrous makes up structural purposes such as hair, skin, muscles etc Keratin in the
• Globular are more specialized in their functions.
Oxygen carriers
Communication (nerves)
 Defence (antibodies)
 Catalyst (enzymes)
• They are used in metabolic processes.

3b) Identify the major functional groups in an amino acid.

• There are 20 amino acids in proteins
• Amino group – NH2 (alkaline properties)
• Carboxylic Acid group –COOH
• The amino is attached to carbon next to acid group.
• R-CH(NH2)-CO2H

3c) Describe the composition and general formula for amino acids and explain that
proteins are chains of amino acids.
• Proteins are long chains of amino acids linked by peptide bonds.
• Proteins are polymeric. Up to 20 amino acids found in a protein.
• Formula is NH2-CH(R)-COOH
• When amino acid link they eliminate a water. They have the elements CHON.
 the amino group one A.A joins to the carboxylic of the other A.A.
The bond between them is known as amide links or peptide bonds.
Two amino acids linked is dipeptide, three is tri peptide. When happens a lot
known as polypeptide.
• Chain of amino acids can be represented by using a three letter code for each
amino acid.
• Most amino acids are zwitterions due to their dipolar structure. (+ end to the
left and – end to the right)

3d) Describe the nature of the peptide bond and explain that proteins can be
broken at different lengths in the chain by choice of enzyme.
• When hydrolysis takes place, the peptide bonds of the protein break apart to
form its component amino acids. (with help of enzyme)
• Protein + water  amino acid
• Un humans and mammals, hydrolysis takes place in digestive system. The
enzyme specifically targets the a.a. and attacks the peptide bond. Therefore
the protein can break down into small length chains without the protein
breaking down to individual amino acids.
• In labs, proteins can either be separated into individual amino acids to
determine its order or be separated into smaller length chain proteins. >e.g.

Gly – Asp + H2O  Gly + Asp (Dipeptide glycylaspartic acid forms glycine and aspartic

3e) Compare the processes of chromatography and electrophoresis and identify the
properties of mixtures that allow them to be separated by either of these processes.
• Chromatography is the name used for separating substances based upon their
differential distribution between two phases, one stationary and the other mobile.
(based on a range of physical and chemical properties)
• Most common type is paper chromatography. This is method of separating
substances based on their different solubilities in a liquid (water usually) trapped
in the pores of paper.
 its separation comes due to the different substances having different solubilities in
the two liquids involved. Water in fibre (stationary phase) and liquid up the paper is
mobile phase.
 High solubility in stat and low in mobile = slower.
 Low solubility in stat and high in mobile = faster
• The degree of solubility of a substance is determined by the polarity of the
substance and the solvent. (therefore the solvent can be altered) Two substances
of similar solubility don’t separate as good.
• Paper chromatography is used more commonly in amino acid separation. A spot
of it is put on starting line. Solvent such as butanol/acetic acid is used to move up
the paper. The amino acid moves through paper at variable rates depending on
their differential solubilities in the two phases. More polar ones dissolve readily
in water phase so move slower. Less polar more soluble in mobile so move faster.
• Electrophoresis separates on the basis of different charges amino acids have in
different pH. In acidic, the amine is protonated give a positive charge and in
alkaline the carboxylic is deprotonated giving it a negative charge.
• Amino acids I solution are in equilibrium therefore called zwitter ions as they are
• In paper one, it is soaked with buffer electrolyte, Mixture put in centre of paper.
Potential difference applied and amino acids move in different directions and
rates. Its different mobility is related to its size, the higher the, the faster the ions
will move.
• Overall, chromatography is based on their different solubilites in polar, non-polar
solvents and in electrophoresis its based on their charge and size.
• For electrophoresis, the charge can vary by change pH of solution and in
chromatography by changing solvent.

3f) Discuss the role of electrophoresis in identifying the origins of protein and
explain how this could assist the forensic chemist.
• Forensic chemists can readily identify proteins by using chromatography and
electrophoresis to determine the proportion and type of each of the amino acids
present. Certain proteins are characteristic of various plant or animal sources.
• It separates individual amino acids in a protein and so therefore the protein can be
• E.g. proteins in red blood cell determine its blood groups. When electrophoresis
identifies the A.A it identifies the protein and so therefore determines the blood
group in which the forensic chemist can use it as collaborative evidence.

3B) Distinguishing tests for proteins.

Test Method
Ninhydrin Add ninhydrin (colourless) Purple colour
shows there is protein or amino acid
Biuret Add Copper Sulfate to alkaline sample.
Purple shows proteins or peptides but not
amino acids
4a) Outline the structure and composition of DNA

• DNA = Deoxyribonucleic Acid (acidic due to phosphate) They are made of

nucleotides into long chain polymers.
• Makes up the genetic code and is found in nucleus
• P-SB
• DNA is two of these chains twisted to form a double helix. It is complementary
so therefore the number of C=G and A=T.

• It carries genetic information that determines nature of cell regulates growth and
division and controls synthesis of enzymes and other proteins.

• Hydrogen bonding keeps the helixes together…it’s a very strong bond but is the
weakest of them all.
4b) Explain why analysis of DNA allows identification of individuals.
• Due to similarity in species, most of our DNA is the same however there are
• People have unique DNA from the non-coding bits that separates the genes.
• The coding sequences along the genes are called exons and non coding ones are
known as introns (junk DNA). These introns vary from people to people and it is
these parts used in identification in forensics.
• Related people show similar introns. (introns carried on the series of bases).

4c) Describe the process used to anaylse DNA and account for its use in:
Identifying relationships between people and identify individuals.
• Any process used to identify DNA sequence is known as DNA fingerprinting.
• It is used for identifying someone who produced a biological sample at a crime
scene. E.g. sperm, saliva, hair, skin
• Identifying father in paternity tests.
• Establishing familial links.
4A) Discuss the range of uses of DNA analysis in forensic chemistry and use
available evidence in discussing the issues associated with its use in terms of the
ethics of maintenance of data banks of DNA.
• DNA testing allows for
1. Identification of individual who’s DNA collected at a crime scene
2. Identifying the victim
3. Identifying unknown body/body part
4. Identifying whether a species is human or not.
5. Father in paternity cases
6. Family members
7. Archeological remains.
• Two ways of being stored, DNA directly because it is stable if kept under right
conditions or just storing results of DNA profile.
• Australia one is CrimTrac July 2001 and samples taken from every prisoner and
• Invasion of privacy
• Genetic discrimination by Govt, employers, schools,
• Storing it
• Choice of what is stored
• It can be tampered with

• Identification of ppl responsible.
• Identification of ppl incorrectly suspected.
• Provides more accurate results.

5a) Explain what is meant by the destructive testing of material and explain why
this may be a problem to forensic investigations.
• Non-destructive is optical methods such as photography, microscopy and
spectroscopic ways such as UV, infrared.
• Destructive is mass spectrometry and separation such as thin layer chromat, GLC
and HPLC.
 something is destructive if it modifies the sample. These are things such as
reversible reactions and separations. It is good to know that the reliability of a sample
in its original way is vital in the court as it allows for re-analysis.
• If the original sample is not recoverable, the analysis is called a destructive
analysis. These involve heating burning. Therefore it is necessary that non
destructive ways are used first.
• Sometimes destructive isn’t allowed such as identifying artworks and historical
facts or that metal in jewelry is precious.
• The problems of small samples and non destructive testing creates difficulties.

5b) Identify, outline and assess the value of the following techniques in the analysis
of small samples, GLC and HPLC.

• This is fast separation of complex mixtures and allows for quantitive
determination if each compound.
• It is very sensitive and can detect drugs in Urine samples.
1. A sample brought in by syringe
2. Into heated injection chamber
3. Nitrogen gas flows trough carrying sample into the column
4. Column has thin film of liquid
5. After separation the carried gas and separate mixture flows in detector which
activates a recorder
6. Traces a series of peaks on chromatogram

• Allows sensitive analysis of range of compounds and used for pharmaceutical
• Others such as cosmetics, explosives, soft drinks, herbicides and drinking water.

1. Components can be identified by comparing it with their retention time of known

standards under same conditions
2. Quantitive info can be obtained under area under peak of chromatogram.

• Asses: limitations of instrument, sample size and reliability

• Used for analysis of poisons in autopsy (HPLC), inks in forge banknotes

5c) Outline how a mass spectrometer operates and clarify its use for forensic
• This is form of analysis that separates and identifies substances on the basis of the
masses of the positive ions formed by the substances when they are bombarded by
high-energy particles (electrons) in high vacuum.
• It depends on mass to charge ratio of ionized atoms.
1. Samples vapourised
2. the sample then passes through an inlet into ionic chamber (low pressure).
An electron beam ionizes part of sample by knocking out electrons from
neutral atoms to form ions with single +ve charge.
3. Positive ions accelerated to high speeds by electric field.
4. Then pass though perpendicular magnetic field. Causes ions o move in a
curve with radius depending on m/e ratio.
5. Ions with particular radius will reach the collector.
6. The detector identifies its mass from its path and these are recorded as a
mass spectrum.
• Mass spectra’s are unique. Computers can be used to match unknowns with
standards if spectra’s are stored electronically which is major use of it by forensic
• It can analyse for enhancing drugs in sport
• Particular ratio of isotopes may be characteristic of particular sites under forensic
• Need to identify objects or residues left at crime scenes.

6a) Describe the conditions under which atoms will emit light.
• When an electron in an allowed high energy (exited) orbital falls to a lower
energy (ground state) orbital as the energy is emitted in form of light.
• The light emitters are in a single whole quantum (hv) of energy or a photon of
• Big jumps release U.V.-medium releases visible light-small release I.R. radiation.
• Energy that an electron has is not variable, there are only certain values of energy
that the electron can have. We therefore say that the energy is quantized meaning
that the energy that the electron can possess must be discrete whole number
multiples of a basic ‘parcel’ of energy called a quantum.

6b)Identify that the emission if quanta of energy as electrons move to lower energy
levels may be detected by humans as a specific colour.
• White light is all colors combined. Spectrum can split into 3 – UV, white, I.R.
• Each colour corresponds to a wavelength. Red has longer than blue
• The wavelength is proportional to energy released. Therefore, as amount of
energy released decreases, wavelength increases.
• Humans see this as colour.

6c) Explain why excited atoms in the gas phase emit or absorb only certain
wavelengths of light.
• The emission spectrum of each element occurs as a result of electrons moving
between the elements electronic levels, reflecting its structure.
• All levels have different energy values so transitions between pairs involve
different energy changes so light emission are at different wavelengths. Therefore
emission spectra of elements are diff.
• Each excited atom emits 1 wavelength. Not all atoms will absorb or be excited in
the same way and so excited atoms will travel to different energy levels (diff
distances from ground state)
• Each element produces different wavelengths of light as each element has a
unique energy level system (energy shell spacing). Therefore according to the
element, electrons will travel to different shells.

6d) Account for the fact that each elements produces its signature line emission
• When light analysed by spectroscopy, it is separated to its colours. The individual
colours are separated to form individual lines which are representatives of the
wavelengths of colour formed by the emission of energy from particular element.
• Each element has a unique combination of color wavelength and so a specific
series of lines are formed. Thee are known as spectrum.
6e) Discuss the use of line emission spectra to identify the presence of elements in
• Detect presence of small levels of contaminants such as soil and water. (crime
• Monitor concentration of many elements in water especially metals.
• Used for soil analyses (agricultural and criminal) purposes.